ArticleThe Journal of biological chemistry2013
ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- ADAMDEC1 predicts prognosis and immunotherapy response in a pan-cancer study with experimental validation.Discover oncology · 2026Article
- Identification and validation of KLRB1-related biomarkers in rheumatoid arthritis.Scientific reports · 2026Article
- ADAMDEC1 promotes cervical squamous cell carcinoma by enhancing the JAK/STAT signaling pathway through modulation of TYMP.Naunyn-Schmiedeberg's archives of pharmacology · 2025Article
- A transcriptome-wide association study integrating multi-omics bioinformatics and Mendelian randomization reveals the prognostic value of ADAMDEC1 in colon cancer.Archives of toxicology · 2025Article
- ADAMDEC1 promotes the malignant progression of cholangiocarcinoma by regulating NF-κB signaling pathway.Scientific reports · 2025Article
- A Lacticaseibacillus rhamnosus secretome induces immunoregulatory transcriptional, functional and immunometabolic signatures in human THP-1 monocytes.Scientific reports · 2024Article
- Exploring FeLV-Gag-Based VLPs as a New Vaccine Platform-Analysis of Production and Immunogenicity.International journal of molecular sciences · 2023Article
- Metalloendopeptidase ADAM-like Decysin 1 (ADAMDEC1) in Colonic Subepithelial PDGFRαInternational journal of molecular sciences · 2022Article
- Upregulation of ADAMDEC1 correlates with tumor progression and predicts poor prognosis in non-small cell lung cancer (NSCLC) via the PI3K/AKT pathway.Thoracic cancer · 2022Article
- Colon stroma mediates an inflammation-driven fibroblastic response controlling matrix remodeling and healing.PLoS biology · 2022Article
- ADAMDEC1 accelerates GBM progressionFrontiers in oncology · 2022Article
- Knockdown of ADAMDEC1 inhibits the progression of glioma in vitro.Histology and histopathology · 2020Article
- ADAMDEC1 Maintains a Growth Factor Signaling Loop in Cancer Stem Cells.Cancer discovery · 2019Article
- Potential early clinical stage colorectal cancer diagnosis using a proteomics blood test panel.Clinical proteomics · 2019Article
- MCSF drives regulatory DC development in stromal co-cultures supporting hematopoiesis.BMC immunology · 2018Article
- ADAM-like Decysin-1 (ADAMDEC1) is a positive regulator of Epithelial Defense Against Cancer (EDAC) that promotes apical extrusion of RasV12-transformed cells.Scientific reports · 2018Article
- Article
- The soluble protease ADAMDEC1 released from activated platelets hydrolyzes platelet membrane pro-epidermal growth factor (EGF) to active high-molecular-weight EGF.The Journal of biological chemistry · 2017Article
- Critical Role of the Disintegrin Metalloprotease ADAM-like Decysin-1 [ADAMDEC1] for Intestinal Immunity and Inflammation.Journal of Crohn's & colitis · 2016Article
- Evidence for restricted reactivity of ADAMDEC1 with protein substrates and endogenous inhibitors.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ADAMDEC1 (Decysin-1) is a putative ADAM (a disintegrin and metalloprotease)-like metalloprotease with an unknown physiological role, selectively expressed in mature dendritic cells and macrophages. When compared with other members of the ADAM family, ADAMDEC1 displays some unusual features. It lacks the auxiliary cysteine-rich, EGF, and transmembrane domains, as well as the cytoplasmic tail. The active site of ADAMDEC1 is unique by being the only mammalian ADAM protease with a non-histidine zinc ligand, having an aspartic acid residue instead. Here we demonstrate that ADAMDEC1, despite these unique features, functions as an active metalloprotease. Thus, ADAMDEC1 is secreted as a mature, glycosylated, and proteolytically active metalloprotease, capable of cleaving macromolecular substrates. In the recombinant form, three of the four potential N-linked glycosylation sites are modified by carbohydrate attachment. Substitution of basic residues at the predicted proprotein convertase cleavage site blocks proprotein processing, revealing both specific ADAMDEC1-dependent and specific ADAMDEC1-independent cleavage of the prodomain. The pro-form of ADAMDEC1 does not have proteolytic activity, demonstrating that the prodomain of ADAMDEC1, like in other members of the ADAM family, confers catalytic latency. Interestingly, the proteolytic activity of mature ADAMDEC1 can be significantly enhanced when a canonical ADAM active site with three zinc-coordinating histidine residues is introduced.
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